Protein methylation and interaction with the antiproliferative gene, BTG2/TIS21/Pc3.

The last one and half a decade witnessed an outstanding re-emergence of attention and remarkable progress in the field of protein methylation. In the present article, we describe the early discoveries in research and review the role protein methylation played in the biological function of the antiproliferative gene, BTG2/TIS21/PC3.

Historical review: the field of protein methylation.

Although the field of protein methylation enjoys widespread interest in the scientific literature of today, this is a recent phenomenon. Papers on 'protein methylation' were first published in the 1960s. By the early 1980s, it was known that lysine, arginine, histidine and dicarboxylic amino acids were post-translationally methylated by highly specific methyltransferases.

Multimerization of expressed protein-arginine methyltransferases during the growth and differentiation of rat liver.

Protein-arginine methylation is a posttranslational modification which yields monomethyl and dimethyl (asymmetric or symmetric) arginines in proteins. We investigated the expressions of PRMT1 and PRMT5 in relation to their catalytic activities in rat liver during growth and differentiation as well as in the pancreas. Western immunoblot analysis revealed that both PRMT1 and PRMT5 proteins were expressed in the cytosol of liver and pancreas with molecular mass of about 42 kDa and 72 kDa, respectively.

Increased methylation of endogenous 20-kDa protein in HIT beta-cell during insulin secretion.

Enzymatic methylation of endogenous proteins in clonal pancreatic beta-cell, HIT-T15, was investigated. When cell extract incubated with S-adenosyl-L-[methyl-3H]methionine was subjected to SDS-PAGE followed by fluorography, endogenous 20-kDa protein was highly [methyl-3H]-labeled. The increase of methylation was correlated with insulin secretion, when the cells were treated with secretagogue; at 5.

Induction of thermal and chemical stability of O6-methylguanine-DNA methyltransferase by Ca2+.

Divalent cations stabilized rat recombinant O6-methylguanine-DNA methyltransferase (rMGMT) protein against heat treatment. Activity of rMGMT was completely abolished by incubating at 45 degrees C for 30 min, however, addition of 1.0 mM Mg2+, Ca2+ or Mn2+ significantly protected heat-induced inactivation of MGMT activity (50-60% vs.